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-Structure paper
Title | Structural basis of translation termination, rescue, and recycling in mammalian mitochondria. |
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Journal, issue, pages | Mol Cell, Vol. 81, Issue 12, Page 2566-22582.e6, Year 2021 |
Publish date | Jun 17, 2021 |
Authors | Eva Kummer / Katharina Noel Schubert / Tanja Schoenhut / Alain Scaiola / Nenad Ban / |
PubMed Abstract | The mitochondrial translation system originates from a bacterial ancestor but has substantially diverged in the course of evolution. Here, we use single-particle cryo-electron microscopy (cryo-EM) as ...The mitochondrial translation system originates from a bacterial ancestor but has substantially diverged in the course of evolution. Here, we use single-particle cryo-electron microscopy (cryo-EM) as a screening tool to identify mitochondrial translation termination mechanisms and to describe them in molecular detail. We show how mitochondrial release factor 1a releases the nascent chain from the ribosome when it encounters the canonical stop codons UAA and UAG. Furthermore, we define how the peptidyl-tRNA hydrolase ICT1 acts as a rescue factor on mitoribosomes that have stalled on truncated messages to recover them for protein synthesis. Finally, we present structural models detailing the process of mitochondrial ribosome recycling to explain how a dedicated elongation factor, mitochondrial EFG2 (mtEFG2), has specialized for cooperation with the mitochondrial ribosome recycling factor to dissociate the mitoribosomal subunits at the end of the translation process. |
External links | Mol Cell / PubMed:33878294 |
Methods | EM (single particle) |
Resolution | 3.2 - 4.6 Å |
Structure data | EMDB-12527, PDB-7nqh: EMDB-12529, PDB-7nql: EMDB-12567, PDB-7nsh: EMDB-12568, PDB-7nsi: EMDB-12569, PDB-7nsj: |
Chemicals | ChemComp-MG: ChemComp-ZN: ChemComp-SPM: ChemComp-GTP: ChemComp-5GP: ChemComp-HOH: ChemComp-GNP: |
Source |
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Keywords | TRANSLATION / Ribosome / Mitochondria / Termination / mtRF1a / Release / ICT1 / mtRRF / Recycling / tRNA(E*) |